Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q2YQM7 (PDXJ_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxine 5'-phosphate synthase

Short name=PNP synthase
EC=2.6.99.2
Gene names
Name:pdxJ
Ordered Locus Names:BAB1_1404
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length246 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5'-phosphate (PNP) and inorganic phosphate By similarity. HAMAP-Rule MF_00279

Catalytic activity

1-deoxy-D-xylulose 5-phosphate + 3-amino-2-oxopropyl phosphate = pyridoxine 5'-phosphate + phosphate + 2 H2O. HAMAP-Rule MF_00279

Pathway

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 5/5. HAMAP-Rule MF_00279

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_00279

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00279.

Sequence similarities

Belongs to the PNP synthase family.

Ontologies

Keywords
   Biological processPyridoxine biosynthesis
   Cellular componentCytoplasm
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpyridoxine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionpyridoxine 5'-phosphate synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 246246Pyridoxine 5'-phosphate synthase HAMAP-Rule MF_00279
PRO_0000231791

Regions

Region221 – 22223-amino-2-oxopropyl phosphate binding By similarity

Sites

Active site441Proton acceptor By similarity
Active site761Proton acceptor By similarity
Active site1981Proton donor By similarity
Binding site813-amino-2-oxopropyl phosphate By similarity
Binding site1913-amino-2-oxopropyl phosphate By similarity
Binding site4611-deoxy-D-xylulose 5-phosphate By similarity
Binding site5111-deoxy-D-xylulose 5-phosphate By similarity
Binding site10611-deoxy-D-xylulose 5-phosphate By similarity
Binding site19913-amino-2-oxopropyl phosphate; via amide nitrogen By similarity
Site1571Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YQM7 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 7AEF11306AE7B475

FASTA24626,466
        10         20         30         40         50         60 
MPAKLSVNLN AIAMLRNRRD LPWPSVTGLG RAALAAGAAG LTVHPRPDQR HIRFSDLGDI 

        70         80         90        100        110        120 
RALIDDEYPQ AEFNIEGFPS EAFLDLVEKH EPEQVTLVPD DPMQATSDHG WDFMSKADFL 

       130        140        150        160        170        180 
APIVARLKGR GMRVSLFADP DSLGYERAKA IGADRVELYT GPYGATHDDP AAAARELDRL 

       190        200        210        220        230        240 
EKAARAATAL GLAVNAGHDL TVDNLPALVK RIPQLAEVSI GHGLTADALM YGIPVTVSRY 


ITALAG 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ11360.1.
RefSeqYP_414776.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YQM7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_1404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ11360; CAJ11360; BAB1_1404.
GeneID3787970.
KEGGbmf:BAB1_1404.
PATRIC17845792. VBIBruMel86222_1459.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0854.
HOGENOMHOG000258095.
KOK03474.
OMANFEMAAT.
OrthoDBEOG6M9F0H.
ProtClustDBPRK05265.

Enzyme and pathway databases

BioCycBABO359391:GKDV-1434-MONOMER.
BMEL359391:GJOQ-1434-MONOMER.
UniPathwayUPA00244; UER00313.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00279. PdxJ.
InterProIPR013785. Aldolase_TIM.
IPR004569. PyrdxlP_synth_PdxJ.
[Graphical view]
PfamPF03740. PdxJ. 1 hit.
[Graphical view]
SUPFAMSSF63892. SSF63892. 1 hit.
TIGRFAMsTIGR00559. pdxJ. 1 hit.
ProtoNetSearch...

Entry information

Entry namePDXJ_BRUA2
AccessionPrimary (citable) accession number: Q2YQM7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: February 7, 2006
Last modified: February 19, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names